SCOPe 2.04: Domain d1bzlb1: 1bzl B:5-169,B:287-357

Lineage for d1bzlb1 (1bzl B:5-169,B:287-357)

1. Root: SCOPe 2.04

2. Class c: Alpha and beta proteins (a/b) [51349] (148 folds)

3. Fold c.3: FAD/NAD(P)-binding domain [51904] (1 superfamily)
   core: 3 layers, b/b/a; central parallel beta-sheet of 5 strands, order 32145; top antiparallel beta-sheet of 3 strands, meander

4. Superfamily c.3.1: FAD/NAD(P)-binding domain [51905] (9 families)

5. Family c.3.1.5: FAD/NAD-linked reductases, N-terminal and central domains [51943] (15 proteins)
   duplication: both domains have similar folds and functions
   most members of the family contain common C-terminal alpha+beta domain

6. Protein Trypanothione reductase [51947] (2 species)

7. Species Trypanosoma cruzi [TaxId:5693] [51949] (4 PDB entries)

8. Domain d1bzlb1: 1bzl B:5-169,B:287-357 [30523]
   Other proteins in same PDB: d1bzla3, d1bzlb3
   complexed with fad, gcg

Details for d1bzlb1

PDB Entry: 1bzl, 2.4 Å

PDB Description: crystal structure of trypanosoma cruzi trypanothione reductase in complex with trypanothione, and the structure-based discovery of new natural product inhibitors

PDB Compounds: (B:) trypanothione reductase (oxidized form)

SCOPe Domain Sequences for d1bzlb1:

Sequence; same for both SEQRES and ATOM records:

>d1bzlb1 c.3.1.5 (B:5-169,B:287-357) Trypanothione reductase {Trypanosoma cruzi [TaxId: 5693]}
ifdlvvigagsggleaawnaatlykkrvavidvqmvhgppffsalggtcvnvgcvpkklm
vtgaqymehlresagfgwefdrttlraewknliavkdeavlninksydemfrdtegleff
lgwgslesknvvnvresadpasavkerletehillasgswphmpnXgrsprtkdlqlqna
gvmiknggvqvdeysrtnvsniyaigdvtnrvmltpvaineaaalvdtvfgttprkt

Timeline for d1bzlb1:

• d1bzlb1 first appeared (with stable ids) in SCOP 1.55
  
• d1bzlb1 appears in SCOPe 2.03
  
• d1bzlb1 appears in SCOPe 2.05
  
• d1bzlb1 appears in the current release, SCOPe 2.08